RplK

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Gene name rplK
Synonyms relC, tsp
Essential no PubMed
Product ribosomal protein L11 (BL11)
Function translation
Gene expression levels in SubtiExpress: rplK
Interactions involving this protein in SubtInteract: RplK
MW, pI 14 kDa, 9.718
Gene length, protein length 423 bp, 141 aa
Immediate neighbours nusG, rplA
Sequences Protein DNA DNA_with_flanks
Genetic context
RplK context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RplK expression.png















Categories containing this gene/protein

translation, universally conserved proteins, phosphoproteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU01020

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • phosphorylated on Arg-94 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1FOX (C-terminal domain, Geobacillus stearothermophilus), 2FOW (RNA binding domain in complex with RNA, Geobacillus stearothermophilus)
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • Regulatory mechanism:
  • Additional information:
    • The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Sascha Baumann, Sebastian Schoof, Marcel Bolten, Claudia Haering, Motoki Takagi, Kazuo Shin-ya, Hans-Dieter Arndt
Molecular determinants of microbial resistance to thiopeptide antibiotics.
J Am Chem Soc: 2010, 132(20);6973-81
[PubMed:20441189] [WorldCat.org] [DOI] (I p)

Matthew A Lauber, William E Running, James P Reilly
B. subtilis ribosomal proteins: structural homology and post-translational modifications.
J Proteome Res: 2009, 8(9);4193-206
[PubMed:19653700] [WorldCat.org] [DOI] (P p)

Christine Eymann, Georg Homuth, Christian Scharf, Michael Hecker
Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis.
J Bacteriol: 2002, 184(9);2500-20
[PubMed:11948165] [WorldCat.org] [DOI] (P p)

S Zhang, J M Scott, W G Haldenwang
Loss of ribosomal protein L11 blocks stress activation of the Bacillus subtilis transcription factor sigma(B).
J Bacteriol: 2001, 183(7);2316-21
[PubMed:11244072] [WorldCat.org] [DOI] (P p)

B Wienen, R Ehrlich, M Stöffler-Meilicke, G Stöffler, I Smith, D Weiss, R Vince, S Pestka
Ribosomal protein alterations in thiostrepton- and Micrococcin-resistant mutants of Bacillus subtilis.
J Biol Chem: 1979, 254(16);8031-41
[PubMed:112097] [WorldCat.org] (P p)